Previous HGNC Symbols for GLRA1 Gene

Previous GeneCards Identifiers for GLRA1 Gene

Summaries for GLRA1 Gene

Entrez Gene Summary for GLRA1 Gene

The protein encoded by this gene is a subunit of a pentameric inhibitory glycine receptor, which mediates postsynaptic inhibition in the central nervous system. Defects in this gene are a cause of startle disease (STHE), also known as hereditary hyperekplexia or congenital stiff-person syndrome. Multiple transcript variants encoding different isoforms have been found. [provided by RefSeq, Dec 2015]

Tocris Summary for GLRA1 Gene

Glycine receptors (GlyR) are members of the cys-loop family of ligand-gated ion channels, responsible for mediating the inhibitory effects of glycine. They are widely distributed throughout the CNS, particularly within the hippocampus, spinal cord and brain stem.

Protein details for GLRA1 Gene (UniProtKB/Swiss-Prot)

Protein attributes for GLRA1 Gene

Size:

457 amino acids

Molecular mass:

52624 Da

Quaternary structure:

Homopentamer (in vitro) (PubMed:22715885, PubMed:22973015, PubMed:23994010, PubMed:25730860). Interacts with GLRB to form heteropentameric channels; this is probably the predominant form in vivo (PubMed:22715885, PubMed:22973015, PubMed:25445488). Heteropentamer composed of two GLRA1 and three GLRB (PubMed:22715885). Heteropentamer composed of three GLRA1 and two GLRB (PubMed:22973015). Both homopentamers and heteropentamers form functional ion channels, but their characteristics are subtly different (PubMed:14551753, PubMed:22715885, PubMed:22973015, PubMed:25445488, PubMed:23994010, PubMed:25730860).

Suggested Antigen Peptide Sequences for GLRA1 Gene

Graphical View of Domain Structure for InterPro Entry

UniProtKB/Swiss-Prot:

The channel pore is formed by pentameric assembly of the second transmembrane domain from all five subunits. In the absence of the extracellular domain, the channel is in a constitutively open conformation (PubMed:23994010). Channel opening is effected by an outward rotation of the transmembrane domains that increases the diameter of the pore (By similarity).

The channel pore is formed by pentameric assembly of the second transmembrane domain from all five subunits. In the absence of the extracellular domain, the channel is in a constitutively open conformation (PubMed:23994010). Channel opening is effected by an outward rotation of the transmembrane domains that increases the diameter of the pore (By similarity).